Abstract
Skin aging can be classified into two types: intrinsic aging and photoaging [1]. Intrinsic aging is the basic biological process common to all living things and is characterized as an age-dependent deterioration of skin functions and structures, such as epidermal atrophy and epidermal–dermal junctional flattening [2]. Photoaging is well known to be a consequence of chronic exposure of the skin to sunlight. Sun-exposed skin, such as face or neck skin, clearly appears to be “prematurely aged” in comparison with the relatively sun-protected skin of the trunk or thigh, and is characterized by various clinical features, including wrinkles, sagging, roughness, sallowness, pigmentary changes, telangiectasis, and neoplasia [3, 4]. The histological features of sun-exposed skin include cellular atypia, loss of polarity, flattening of the dermal–epidermal junctions (DEJ), a decrease in collagen, and dermal elastosis [2, 5].
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Tagami H. Functional characteristics of the stratum corneum in photoaged skin in comparison with those found in intrinsic aging. Arch Dermatol Res. 2008;300(S1):1–6.
Lavker RM. Structural alterations in exposed and unexposed aged skin. J Invest Dermatol. 1979;73:59–66.
Gilchrest BA. Skin aging and photoaging: an overview. J Am Acad Dermatol. 1989;21:610–613.
Griffiths CE. The clinical identification and quantification of photodamage. Br J Dermatol. 1992;127(41):37–42.
Kligman AM, Grove GL, Hirose R, et al. Topical tretinoin for photoaged skin. J Am Acad Dermatol. 1986;15:836–859.
Ryan MC, Christiano AM, Engvall E, et al. The functions of laminins: lessons from in vivo studies. Matrix Biol. 1996;15:369–381.
Bohnert A, Hornung J, Mackenzie IC, et al. Epithelial-mesenchymal interactions control basement membrane production and differentiation in cultured and transplanted mouse keratinocytes. Cell Tissue Res. 1986;244:413–429.
Watt FM. Selective migration of terminally differentiating cells from the basal layer of cultured human epidermis. J Cell Biol. 1984;98:16–21.
Barrandon Y, Green H. Three clonal types of keratinocyte with different capacities for multiplication. Proc Natl Acad Sci USA. 1987;84:2302–2306.
Hirai Y, Takebe K, Takashina M, et al. Epimorphin: a mesenchymal protein essential for epithelial morphogenesis. Cell. 1992;69:471–481.
Inoue S. Ultrastructure of basement membranes. Int Rev Cytol. 1989;117:57–98.
Aberdam D, Galliano MF, Vailly J, et al. Herlitz’s junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma 2 subunit of nicein/kalinin (LAMININ-5). Nat Genet. 1994;6:299–304.
Amano S, Scott IC, Takahara K, et al. Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain. J Biol Chem. 2000;275:22728–22735.
Goldfinger LE, Stack MS, Jones JC. Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator. J Cell Biol. 1998;141:255–265.
Koshikawa N, Minegishi T, Sharabi A, et al. Membrane-type matrix metalloproteinase-1 (MT1-MMP) is a processing enzyme for human laminin gamma 2 chain. J Biol Chem. 2005;280:88–93.
Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol. 1995;7:728–735.
Reynolds JJ. Collagenases and tissue inhibitors of metalloproteinases: a functional balance in tissue degradation. Oral Dis. 1996;2:70–76.
Fassina G, Ferrari N, Brigati C, et al. Tissue inhibitors of metalloproteases: regulation and biological activities. Clin Exp Metastasis. 2000;18:111–120.
Goldberg GI, Marmer BL, Grant GA, et al. Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2. Proc Natl Acad Sci USA. 1989;86:8207–8211.
Sato H, Takino T, Okada Y, et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature. 1994;370:61–65.
Saksela O. Plasminogen activation and regulation of pericellular proteolysis. Biochim Biophys Acta. 1985;823:35–65.
Morioka S, Jensen PJ, Lazarus GS. Human epidermal plasminogen activator. Characterization, localization, and modulation. Exp Cell Res. 1985;161:364–372.
Marschall C, Lengyel E, Nobutoh T, et al. UVB increases urokinase-type plasminogen activator receptor (uPAR) expression. J Invest Dermatol. 1999;113:69–76.
Plow EF, Freaney DE, Plescia J, et al. The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type. J Cell Biol. 1986;103:2411–2420.
Katsuta Y, Yoshida Y, Kawai E, et al. Urokinase-type plasminogen activator is activated in stratum corneum after barrier disruption. J Dermatol Sci. 2003;32:55–57.
Denda M, Kitamura K, Elias PM, et al. Trans-4-(Aminomethyl)cyclohexane carboxylic acid (T-AMCHA), an anti-fibrinolytic agent, accelerates barrier recovery and prevents the epidermal hyperplasia induced by epidermal injury in hairless mice and humans. J Invest Dermatol. 1997;109:84–90.
Bell E, Ehrlich HP, Buttle DJ, et al. Living tissue formed in vitro and accepted as skin-equivalent tissue of full thickness. Science. 1981;211:1052–1054.
Amano S, Akutsu N, Matsunaga Y, et al. Importance of balance between extracellular matrix synthesis and degradation in basement membrane formation. Exp Cell Res. 2001;271:249–262.
Tsunenaga M, Adachi E, Amano S, et al. Laminin 5 can promote assembly of the lamina densa in the skin equivalent model. Matrix Biol. 1998;17:603–613.
Tsunenaga M, Kohno Y, Horii I, et al. Growth and differentiation properties of normal and transformed human keratinocytes in organotypic culture. Jpn J Cancer Res. 1994;85:238–244.
Nishiyama T, Amano S, Tsunenaga M, et al. The importance of laminin 5 in the dermal-epidermal basement membrane. J Dermatol Sci. 2000;24:S51–59.
Feldman D, Bryce GF, Shapiro SS. Mitochondrial inclusions in keratinocytes of hairless mouse skin exposed to UVB radiation. J Cutan Pathol. 1990;17:96–100.
Sarret Y, Woodley DT, Goldberg GS, et al. Constitutive synthesis of a 92-kDa keratinocyte-derived type IV collagenase is enhanced by type I collagen and decreased by type IV collagen matrices. J Invest Dermatol. 1992;99:836–841.
Sudbeck BD, Parks WC, Welgus HG, et al. Collagen-stimulated induction of keratinocyte collagenase is mediated via tyrosine kinase and protein kinase C activities. J Biol Chem. 1994;269:30022–30029.
Amano S, Ogura Y, Akutsu N, et al. Protective effect of matrix metalloproteinase inhibitors against epidermal basement membrane damage: skin equivalents partially mimic photoageing process. Br J Dermatol. 2005;153(2):37–46.
Herrmann G, Wlaschek M, Lange TS, et al. UVA irradiation stimulates the synthesis of various matrix-metalloproteinases (MMPs) in cultured human fibroblasts. Exp Dermatol. 1993;2:92–97.
Kawaguchi Y, Tanaka H, Okada T, et al. The effects of ultraviolet A and reactive oxygen species on the mRNA expression of 72-kDa type IV collagenase and its tissue inhibitor in cultured human dermal fibroblasts. Arch Dermatol Res. 1996;288:39–44.
Brenneisen P, Wenk J, Klotz LO, et al. Central role of Ferrous/Ferric iron in the ultraviolet B irradiation-mediated signaling pathway leading to increased interstitial collagenase (matrix-degrading metalloprotease (MMP)-1) and stromelysin-1 (MMP-3) mRNA levels in cultured human dermal fibroblasts. J Biol Chem. 1998;273:5279–5287.
Koivukangas V, Kallioinen M, Autio-Harmainen H, et al. UV irradiation induces the expression of gelatinases in human skin in vivo. Acta Dermatol Venereol. 1994;74:279–282.
Fisher GJ, Datta SC, Talwar HS, et al. Molecular basis of sun-induced premature skin ageing and retinoid antagonism. Nature. 1996;379:335–339.
Inomata S, Matsunaga Y, Amano S, et al. Possible involvement of gelatinases in basement membrane damage and wrinkle formation in chronically ultraviolet B-exposed hairless mouse. J Invest Dermatol. 2003;120:128–134.
Ogura Y, Matsunaga Y, Nishiyama T, et al. Plasmin induces degradation and dysfunction of laminin 332 (laminin 5) and impaired assembly of basement membrane at the dermal-epidermal junction. Br J Dermatol. 2008;159:49–60.
Miralles F, Parra M, Caelles C, et al. UV irradiation induces the murine urokinase-type plasminogen activator gene via the c-Jun N-terminal kinase signaling pathway: requirement of an AP1 enhancer element. Mol Cell Biol. 1998;18:4537–4547.
Scharffetter K, Wlaschek M, Hogg A, et al. UVA irradiation induces collagenase in human dermal fibroblasts in vitro and in vivo. Arch Dermatol Res. 1991;283:506–511.
Fleischmajer R, Schechter A, Bruns M, et al. Skin fibroblasts are the only source of nidogen during early basal lamina formation in vitro. J Invest Dermatol. 1995;105:597–601.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2010 Springer-Verlag Berlin Heidelberg
About this entry
Cite this entry
Amano, S. (2010). Possible Involvement of Basement Membrane Damage by Matrix Metalloproteinases and Serine Proteinases in Skin Aging Process. In: Farage, M.A., Miller, K.W., Maibach, H.I. (eds) Textbook of Aging Skin. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-89656-2_12
Download citation
DOI: https://doi.org/10.1007/978-3-540-89656-2_12
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-89655-5
Online ISBN: 978-3-540-89656-2
eBook Packages: MedicineReference Module Medicine